Research workbench
Crystal structure of the xiap ring domain
Analyse Crystal structure of the xiap ring domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4IC2
- Type
- protein
- Length
- 126 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- E3 ubiquitin-protein ligase xiap
- EC
- 6.3.2.-
- UniProt
- P98170
- Ligands
- ZN, NI
- Pockets
- 1 · best druggability 0.64
Structure
x-ray diffraction · 2 distinct chains · 22% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | E3 ubiquitin-protein ligase xiap (EC 6.3.2.-) | protein | 62 | 23% helix, 24% strand | P98170 |
| B | E3 ubiquitin-protein ligase xiap (EC 6.3.2.-) | protein | 64 | 22% helix, 27% strand | P98170 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 162 | 0.64 | 0.85 | 20 | empty |
Interfaces
1 interface between chains.
- A–B · 937 Ų buried · 9 hydrogen bonds · protein-protein
Compared structures
- 4IC2 · Crystal structure of the XIAP RING domain · the same entry in another collection · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P98170
- Elsewhere: RCSB PDB 4IC2 · PDBe 4IC2 · UniProt P98170
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.